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Classification and Antihypertensive Activity of Angiotensin I‐Converting Enzyme Inhibitory Peptides Derived from Food Proteins

Iroyukifujita, H, Eiichiyokoyama, K, Yoshikawa, Masaaki·2000·Journal of Food Science

Abstract

ABSTRACT: Angiotensin I‐converting enzyme (ACE)‐inhibitory peptides from the thermolysin digest of chicken muscle and the peptic digest of ovalbumin were isolated. However, some of them failed to show antihypertensive activity in spontaneously hypertensive rats (SHR). To clarify this discrepancy, ACE‐inhibitory peptides from various sources were preincubated with ACE before measurement of ACE‐inhibitory activity and classified into 3 groups: (1) inhibitor type, IC 50 values of peptides that are not affected after preincubation with ACE; (2) substrate type, peptides that are hydrolyzed by ACE to give peptides with weaker activity; and (3) prodrug‐type inhibitor, these peptides are converted to true inhibitors by ACE or gastrointestinal proteases. Peptides belonging to the 1st and the 3rd groups exert antihypertensive activities even after oral administration in SHR.

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Metadata

Authors
Iroyukifujita, H., Eiichiyokoyama, K., & Yoshikawa, M.
Venue
Journal of Food Science
Publisher
Wiley
Published
2000-05
Volume
65
Issue
4
Pages
564-569
ISSN
  • 0022-1147 (ISSN-L)
  • 1750-3841
OpenAlex
W2052418725
Cited by
543
References
0
FWCI
2.82
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Classification and Antihypertensive Activity of Angiotensin I‐Converting Enzyme Inhibitory Peptides Derived from Food Proteins. https://app.cochat.ai/papers/10.1111/j.1365-2621.2000.tb16049.x
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Iroyukifujita, H., Eiichiyokoyama, K., & Yoshikawa, M. (2000). Classification and Antihypertensive Activity of Angiotensin I‐Converting Enzyme Inhibitory Peptides Derived from Food Proteins. Journal of Food Science. https://doi.org/10.1111/j.1365-2621.2000.tb16049.x

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